HEADER ANTIBACTERIAL PROTEIN 06-JUL-91 1COL 1COL 2 COMPND COLICIN *A (C-TERMINAL DOMAIN) (PORE-FORMING DOMAIN) 1COL 3 SOURCE (ESCHERICHIA $COLI) 1COL 4 AUTHOR M.W.PARKER,J.P.M.POSTMA,F.PATTUS,A.D.TUCKER,D.TSERNOGLOU 1COL 5 REVDAT 2 15-JUL-93 1COLA 1 REMARK 1COLA 1 REVDAT 1 15-JUL-92 1COL 0 1COL 6 JRNL AUTH M.W.PARKER,J.P.M.POSTMA,F.PATTUS,A.D.TUCKER, 1COL 7 JRNL AUTH 2 D.TSERNOGLOU 1COL 8 JRNL TITL REFINED STRUCTURE OF THE PORE-FORMING DOMAIN OF 1COL 9 JRNL TITL 2 COLICIN *A AT 2.4 ANGSTROMS RESOLUTION 1COL 10 JRNL REF J.MOL.BIOL. V. 224 639 1992 1COL 11 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 1COL 12 REMARK 1 1COL 13 REMARK 1 REFERENCE 1 1COL 14 REMARK 1 AUTH J.H.LAKEY,D.BATY,F.PATTUS 1COL 15 REMARK 1 TITL FLUORESCENCE ENERGY TRANSFER DISTANCE MEASUREMENTS 1COL 16 REMARK 1 TITL 2 USING SITE-DIRECTED SINGLE CYSTEINE MUTANTS 1COL 17 REMARK 1 REF J.MOL.BIOL. V. 218 639 1991 1COL 18 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1COL 19 REMARK 1 REFERENCE 2 1COL 20 REMARK 1 AUTH F.PATTUS,D.MASSOTTE,H.U.WILMSEN,J.LAKEY, 1COL 21 REMARK 1 AUTH 2 D.TSERNOGLOU,A.TUCKER,M.W.PARKER 1COL 22 REMARK 1 TITL COLICINS: PROKARYOTIC KILLER-PORES 1COL 23 REMARK 1 REF EXPERIENTIA V. 46 180 1990 1COL 24 REMARK 1 REFN ASTM EXPEAM SZ ISSN 0014-4754 018 1COL 25 REMARK 1 REFERENCE 3 1COL 26 REMARK 1 AUTH M.W.PARKER,F.PATTUS,A.D.TUCKER,D.TSERNOGLOU 1COL 27 REMARK 1 TITL STRUCTURE OF THE MEMBRANE-PORE-FORMING FRAGMENT 1COL 28 REMARK 1 TITL 2 OF COLICIN *A 1COL 29 REMARK 1 REF NATURE V. 337 93 1989 1COL 30 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 1COL 31 REMARK 1 REFERENCE 4 1COL 32 REMARK 1 AUTH C.J.LAZDUNSKI,D.BATY,V.GELI,D.CAVARD,J.MORLON, 1COL 33 REMARK 1 AUTH 2 R.LLOUBES.S.P.HOWARD,M.KNIBIEHLER,M.CHARTIER, 1COL 34 REMARK 1 AUTH 3 S.VARENNE,M.FRENETTE,J.-*L.DASSEUX,F.PATTUS 1COL 35 REMARK 1 TITL THE MEMBRANE CHANNEL-FORMING COLICIN *A: SYNTHESIS, 1COL 36 REMARK 1 TITL 2 SECRETION, STRUCTURE, ACTION AND IMMUNITY 1COL 37 REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V. 947 445 1988 1COL 38 REMARK 1 REFN ASTM BBACAQ NE ISSN 0006-3002 113 1COL 39 REMARK 1 REFERENCE 5 1COL 40 REMARK 1 AUTH M.COLLARINI,G.AMBLARD,C.LAZDUNSKI,F.PATTUS 1COL 41 REMARK 1 TITL GATING PROCESSES OF CHANNELS INDUCED BY COLICIN *A, 1COL 42 REMARK 1 TITL 2 ITS C-TERMINAL FRAGMENT AND COLICIN E=1= IN PLANAR 1COL 43 REMARK 1 TITL 3 LIPID BILAYERS 1COL 44 REMARK 1 REF EUR.BIOPHYS.J. V. 14 147 1987 1COL 45 REMARK 1 REFN ASTM EBJOE8 GW ISSN 0175-7571 997 1COLA 2 REMARK 1 REFERENCE 6 1COL 47 REMARK 1 AUTH A.D.TUCKER,F.PATTUS,D.TSERNOGLOU 1COL 48 REMARK 1 TITL CRYSTALLIZATION OF THE C-TERMINAL DOMAIN OF 1COL 49 REMARK 1 TITL 2 COLICIN /A$ CARRYING THE VOLTAGE-DEPENDENT PORE 1COL 50 REMARK 1 TITL 3 ACTIVITY OF THE PROTEIN 1COL 51 REMARK 1 REF J.MOL.BIOL. V. 190 133 1986 1COL 52 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1COL 53 REMARK 2 1COL 54 REMARK 2 RESOLUTION. 2.4 ANGSTROMS. 1COL 55 REMARK 3 1COL 56 REMARK 3 REFINEMENT. MOLECULAR DYNAMICS REFINEMENT BY THE METHOD OF 1COL 57 REMARK 3 M. FUJINAGA, P. GROS, W. F. VAN GUNSTEREN 1COL 58 REMARK 3 (J.APPL.CRYSTALLLOGR., V. 22, P. 1 (1989), PROGRAM 1COL 59 REMARK 3 *GROMOS*) AND BY THE RESTRAINED LEAST-SQUARES PROCEDURE OF 1COL 60 REMARK 3 J. KONNERT AND W. HENDRICKSON (PROGRAM *PROLSQ*). THE R 1COL 61 REMARK 3 VALUE IS 0.18 FOR ALL REFLECTIONS IN THE RESOLUTION RANGE 1COL 62 REMARK 3 6.0 TO 2.4 ANGSTROMS. 1COL 63 REMARK 3 1COL 64 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF 1COL 65 REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED 1COL 66 REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE 1COL 67 REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS) 1COL 68 REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) 1COL 69 REMARK 3 BOND DISTANCE 0.014(0.020) 1COL 70 REMARK 3 ANGLE DISTANCE 0.049(0.040) 1COL 71 REMARK 3 PLANAR 1-4 DISTANCE 0.050(0.045) 1COL 72 REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.011(0.020) 1COL 73 REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.157(0.150) 1COL 74 REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) 1COL 75 REMARK 3 SINGLE TORSION CONTACT 0.244(0.500) 1COL 76 REMARK 3 MULTIPLE TORSION CONTACT 0.374(0.500) 1COL 77 REMARK 3 POSSIBLE HYDROGEN BOND 0.198(0.500) 1COL 78 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES) 1COL 79 REMARK 3 PLANAR (OMEGA) 2.1(3.0) 1COL 80 REMARK 3 STAGGERED 22.1(15.0) 1COL 81 REMARK 3 ORTHONORMAL 31.6(20.0) 1COL 82 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2) 1COL 83 REMARK 3 MAIN-CHAIN BOND 1.8(2.000) 1COL 84 REMARK 3 MAIN-CHAIN ANGLE 2.9(3.000) 1COL 85 REMARK 3 SIDE-CHAIN BOND 5.9(4.500) 1COL 86 REMARK 3 SIDE-CHAIN ANGLE 8.4(6.000) 1COL 87 REMARK 4 1COL 88 REMARK 4 THE TWO MONOMERS IN THE ASYMMETRIC UNIT HAVE BEEN ASSIGNED 1COL 89 REMARK 4 CHAIN INDICATORS *A* AND *B* IN THIS ENTRY. THEY ARE 1COL 90 REMARK 4 RELATED BY A LOCAL DIAD WHICH IS GIVEN ON THE *MTRIX RECORD 1COL 91 REMARK 4 BELOW. THIS TRANSFORMATION WILL YIELD APPROXIMATE 1COL 92 REMARK 4 COORDINATES FOR CHAIN *A* WHEN APPLIED TO CHAIN *B*. 1COL 93 REMARK 5 1COL 94 REMARK 5 RESIDUES 1 - 4 AND 202 - 204 OF EACH CHAIN ARE NOT INCLUDED 1COL 95 REMARK 5 IN THIS ENTRY. 1COL 96 REMARK 6 1COLA 3 REMARK 6 CORRECTION. CORRECT ISSN CODE FOR REFERENCE 5. 1COLA 4 REMARK 6 15-JUL-93. 1COLA 5 SEQRES 1 A 204 VAL ALA GLU LYS ALA LYS ASP GLU ARG GLU LEU LEU GLU 1COL 97 SEQRES 2 A 204 LYS THR SER GLU LEU ILE ALA GLY MET GLY ASP LYS ILE 1COL 98 SEQRES 3 A 204 GLY GLU HIS LEU GLY ASP LYS TYR LYS ALA ILE ALA LYS 1COL 99 SEQRES 4 A 204 ASP ILE ALA ASP ASN ILE LYS ASN PHE GLN GLY LYS THR 1COL 100 SEQRES 5 A 204 ILE ARG SER PHE ASP ASP ALA MET ALA SER LEU ASN LYS 1COL 101 SEQRES 6 A 204 ILE THR ALA ASN PRO ALA MET LYS ILE ASN LYS ALA ASP 1COL 102 SEQRES 7 A 204 ARG ASP ALA LEU VAL ASN ALA TRP LYS HIS VAL ASP ALA 1COL 103 SEQRES 8 A 204 GLN ASP MET ALA ASN LYS LEU GLY ASN LEU SER LYS ALA 1COL 104 SEQRES 9 A 204 PHE LYS VAL ALA ASP VAL VAL MET LYS VAL GLU LYS VAL 1COL 105 SEQRES 10 A 204 ARG GLU LYS SER ILE GLU GLY TYR GLU THR GLY ASN TRP 1COL 106 SEQRES 11 A 204 GLY PRO LEU MET LEU GLU VAL GLU SER TRP VAL LEU SER 1COL 107 SEQRES 12 A 204 GLY ILE ALA SER SER VAL ALA LEU GLY ILE PHE SER ALA 1COL 108 SEQRES 13 A 204 THR LEU GLY ALA TYR ALA LEU SER LEU GLY VAL PRO ALA 1COL 109 SEQRES 14 A 204 ILE ALA VAL GLY ILE ALA GLY ILE LEU LEU ALA ALA VAL 1COL 110 SEQRES 15 A 204 VAL GLY ALA LEU ILE ASP ASP LYS PHE ALA ASP ALA LEU 1COL 111 SEQRES 16 A 204 ASN ASN GLU ILE ILE ARG PRO ALA HIS 1COL 112 SEQRES 1 B 204 VAL ALA GLU LYS ALA LYS ASP GLU ARG GLU LEU LEU GLU 1COL 113 SEQRES 2 B 204 LYS THR SER GLU LEU ILE ALA GLY MET GLY ASP LYS ILE 1COL 114 SEQRES 3 B 204 GLY GLU HIS LEU GLY ASP LYS TYR LYS ALA ILE ALA LYS 1COL 115 SEQRES 4 B 204 ASP ILE ALA ASP ASN ILE LYS ASN PHE GLN GLY LYS THR 1COL 116 SEQRES 5 B 204 ILE ARG SER PHE ASP ASP ALA MET ALA SER LEU ASN LYS 1COL 117 SEQRES 6 B 204 ILE THR ALA ASN PRO ALA MET LYS ILE ASN LYS ALA ASP 1COL 118 SEQRES 7 B 204 ARG ASP ALA LEU VAL ASN ALA TRP LYS HIS VAL ASP ALA 1COL 119 SEQRES 8 B 204 GLN ASP MET ALA ASN LYS LEU GLY ASN LEU SER LYS ALA 1COL 120 SEQRES 9 B 204 PHE LYS VAL ALA ASP VAL VAL MET LYS VAL GLU LYS VAL 1COL 121 SEQRES 10 B 204 ARG GLU LYS SER ILE GLU GLY TYR GLU THR GLY ASN TRP 1COL 122 SEQRES 11 B 204 GLY PRO LEU MET LEU GLU VAL GLU SER TRP VAL LEU SER 1COL 123 SEQRES 12 B 204 GLY ILE ALA SER SER VAL ALA LEU GLY ILE PHE SER ALA 1COL 124 SEQRES 13 B 204 THR LEU GLY ALA TYR ALA LEU SER LEU GLY VAL PRO ALA 1COL 125 SEQRES 14 B 204 ILE ALA VAL GLY ILE ALA GLY ILE LEU LEU ALA ALA VAL 1COL 126 SEQRES 15 B 204 VAL GLY ALA LEU ILE ASP ASP LYS PHE ALA ASP ALA LEU 1COL 127 SEQRES 16 B 204 ASN ASN GLU ILE ILE ARG PRO ALA HIS 1COL 128 FORMUL 3 HOH *83(H2 O1) 1COL 129 HELIX 1 1A GLU A 8 LEU A 30 1 1COL 130 HELIX 2 2A ASP A 32 LYS A 46 1 1COL 131 HELIX 3 3A PHE A 56 THR A 67 1 1COL 132 HELIX 4 AA PRO A 70 MET A 72 1 1COL 133 HELIX 5 4A LYS A 76 LYS A 87 1 1COL 134 HELIX 6 5A ALA A 91 LEU A 101 1 1COL 135 HELIX 7 BA LYS A 103 PHE A 105 1 1COL 136 HELIX 8 6A VAL A 110 THR A 127 1 1COL 137 HELIX 9 7A GLY A 131 LEU A 142 1 1COL 138 HELIX 10 8A SER A 147 SER A 164 1 1COL 139 HELIX 11 9A ALA A 169 ALA A 185 1 1COL 140 HELIX 12 10A LYS A 190 ILE A 199 1 1COL 141 HELIX 13 1B GLU B 8 LEU B 30 1 1COL 142 HELIX 14 2B ASP B 32 LYS B 46 1 1COL 143 HELIX 15 3B PHE B 56 THR B 67 1 1COL 144 HELIX 16 AB PRO B 70 MET B 72 1 1COL 145 HELIX 17 4B LYS B 76 LYS B 87 1 1COL 146 HELIX 18 5B ALA B 91 LEU B 101 1 1COL 147 HELIX 19 BB LYS B 103 PHE B 105 1 1COL 148 HELIX 20 6B VAL B 110 THR B 127 1 1COL 149 HELIX 21 7B GLY B 131 LEU B 142 1 1COL 150 HELIX 22 8B SER B 147 SER B 164 1 1COL 151 HELIX 23 9B ALA B 169 ALA B 185 1 1COL 152 HELIX 24 10B LYS B 190 ILE B 199 1 1COL 153 CRYST1 73.000 73.000 171.600 90.00 90.00 90.00 P 43 21 2 8 1COL 154 ORIGX1 1.000000 0.000000 0.000000 0.00000 1COL 155 ORIGX2 0.000000 1.000000 0.000000 0.00000 1COL 156 ORIGX3 0.000000 0.000000 1.000000 0.00000 1COL 157 SCALE1 0.013699 0.000000 0.000000 0.00000 1COL 158 SCALE2 0.000000 0.013699 0.000000 0.00000 1COL 159 SCALE3 0.000000 0.000000 0.005828 0.00000 1COL 160 MTRIX1 1 0.473450 -0.014580 0.880430 -8.97200 1COL 161 MTRIX2 1 0.025490 -0.999420 -0.030270 90.10000 1COL 162 MTRIX3 1 0.880180 0.036790 -0.473230 15.45200 1COL 163